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Volumn 79, Issue 3, 2000, Pages 1428-1437

Modulation of cytochrome C coupling to anionic lipid monolayers by a change of the phase state: A combined neutron and infrared reflection study

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C OXIDASE; DIMYRISTOYLPHOSPHATIDYLCHOLINE; DIPALMITOYLPHOSPHATIDYLCHOLINE; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLGLYCEROL;

EID: 0033849865     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76394-6     Document Type: Article
Times cited : (20)

References (10)
  • 2
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    • Specular reflection of neutrons at phospholipid monolayers. Changes of monolayer structure and headgroup hydration at the transition from the expanded to the condensed phase state
    • Bayerl, T. M., R. K. Thomas, J. Penfold, A. R. Rennie, and E. Sackmann. 1990. Specular reflection of neutrons at phospholipid monolayers. Changes of monolayer structure and headgroup hydration at the transition from the expanded to the condensed phase state. Biophys. J. 57: 1095-1098.
    • (1990) Biophys. J. , vol.57 , pp. 1095-1098
    • Bayerl, T.M.1    Thomas, R.K.2    Penfold, J.3    Rennie, A.R.4    Sackmann, E.5
  • 5
    • 0027997604 scopus 로고
    • Conformational changes of the lecithin headgroup in monolayers at the air/water interface. A neutron reflection study
    • Brumm, T., C. Naumann, E. Sackmann, A. R. Rennie, R. K. Thomas, D. Kanellas, J. Penfold, and T. M. Bayerl. 1994. Conformational changes of the lecithin headgroup in monolayers at the air/water interface. A neutron reflection study. Eur. Biophys. J. 23:289-296.
    • (1994) Eur. Biophys. J. , vol.23 , pp. 289-296
    • Brumm, T.1    Naumann, C.2    Sackmann, E.3    Rennie, A.R.4    Thomas, R.K.5    Kanellas, D.6    Penfold, J.7    Bayerl, T.M.8
  • 6
    • 0025007598 scopus 로고
    • High-resolution three-dimensional structure of horse heart cytochrome c
    • Bushnell, G. W., and G. V. Louie. 1990. High-resolution three-dimensional structure of horse heart cytochrome c. J. Mol. Biol. 214:585-595.
    • (1990) J. Mol. Biol. , vol.214 , pp. 585-595
    • Bushnell, G.W.1    Louie, G.V.2
  • 7
    • 0016797947 scopus 로고
    • Estimation of amino acid residue side chain absorption in the infrared spectra of protein solutions in heavy water
    • Chirgadze, Y. N., O. V. Fedorov, and N. P. Trushina. 1975. Estimation of amino acid residue side chain absorption in the infrared spectra of protein solutions in heavy water. Biopolymers. 14:679-694.
    • (1975) Biopolymers. , vol.14 , pp. 679-694
    • Chirgadze, Y.N.1    Fedorov, O.V.2    Trushina, N.P.3
  • 8
    • 33845373695 scopus 로고
    • Quantitative external reflection infrared spectroscopic analysis of insoluble monolayers spread at the air-water interface
    • Dluhy, R. A. 1986. Quantitative external reflection infrared spectroscopic analysis of insoluble monolayers spread at the air-water interface. J. Phys. Chem. 90:1373-1379.
    • (1986) J. Phys. Chem. , vol.90 , pp. 1373-1379
    • Dluhy, R.A.1
  • 9
    • 0028237335 scopus 로고
    • External reflection FTIR of peptide monolayer films in situ at the air/water interface: Experimental design, spectra-structure correlations and effects of hydrogen-deuterium exchange
    • Flach, C. R., J. W. Brauner, J. W. Taylor, R. C. Baldwin, and R. Mendelsohn. 1994. External reflection FTIR of peptide monolayer films in situ at the air/water interface: experimental design, spectra-structure correlations and effects of hydrogen-deuterium exchange. Biophys. J. 67: 402-404.
    • (1994) Biophys. J. , vol.67 , pp. 402-404
    • Flach, C.R.1    Brauner, J.W.2    Taylor, J.W.3    Baldwin, R.C.4    Mendelsohn, R.5
  • 10
    • 0031954980 scopus 로고    scopus 로고
    • Direct detection of domains in phospholipid bilayers by grazing incidence diffraction of neutrons and atomic force microscopy
    • Gliss, C., H. Clausen-Schaumann, R. Günther, S. Odenbach, O. Randl, and T. M. Bayerl. 1998. Direct detection of domains in phospholipid bilayers by grazing incidence diffraction of neutrons and atomic force microscopy. Biophys. J. 74:2443-2450.
    • (1998) Biophys. J. , vol.74 , pp. 2443-2450
    • Gliss, C.1    Clausen-Schaumann, H.2    Günther, R.3    Odenbach, S.4    Randl, O.5    Bayerl, T.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.